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rdf:type |
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lifeskim:mentions |
umls-concept:C0013902,
umls-concept:C0026336,
umls-concept:C0026882,
umls-concept:C0030956,
umls-concept:C0037799,
umls-concept:C0205145,
umls-concept:C0205174,
umls-concept:C0205214,
umls-concept:C0205245,
umls-concept:C0332120,
umls-concept:C0332281,
umls-concept:C0332307,
umls-concept:C0443203,
umls-concept:C0596311,
umls-concept:C0597304,
umls-concept:C1330957,
umls-concept:C1704258,
umls-concept:C2003941,
umls-concept:C2674229
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pubmed:issue |
3
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pubmed:dateCreated |
1992-4-7
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pubmed:abstractText |
We studied nine individuals from five unrelated families with alpha I/46-50a hereditary elliptocytosis (HE) or hereditary pyropoikilocytosis (HPP), including one of the original HHP probands first reported by Zarkowsky and colleagues (1975. Br. J. Haematol. 29:537-543). Biochemical analysis of erythrocyte membrane proteins from these patients revealed, as a common abnormality, the presence of the alpha I/46-50a peptide after limited tryptic digestion of spectrin. The polymerase chain reaction was utilized to study the structure of the DNA encoding the alpha I domain of spectrin in the affected individuals. The DNA sequence of the alpha-spectrin gene encoding the region of the alpha-spectrin chain surrounding the abnormal proteolytic cleavage site was normal. We identified a point mutation causing the replacement of a highly conserved leucine residue by proline at position 207 in the alpha-spectrin chain, a site 51 residues to the amino-terminal side of the abnormal proteolytic cleavage site. Analysis of the proposed triple helical model of spectrin repeats reveals that the mutation occurs in helix 2 at a position directly opposite the abnormal proteolytic cleavage site in helix 3, making this the first report of a mutation occurring in helix 2 of a repeat in the alpha I domain of spectrin. These results add to the molecular heterogeneity of mutations associated with HE/HPP and provide further support for the proposed triple helical model of spectrin. Disruption of this proposed alpha-helical structure by helix-breaking proline substitutions may result in a functionally defective spectrin chain.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/1541680-1191563,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1541680-1679439,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/1541680-2568862,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/1541680-2794061,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1541680-2884629,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1541680-3167214,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/1541680-3276733,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1541680-3332099,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1541680-3337911,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1541680-3359047,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1541680-3580577,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1541680-3597773,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1541680-3611052,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1541680-3620700,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/1541680-4052329,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1541680-4326772,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1541680-5432063,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1541680-6472478,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1541680-6493844,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/1541680-689023,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/1541680-7003593,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1541680-7059678,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1541680-7096353,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1541680-7099765,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1541680-7119110
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
AIM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0021-9738
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
89
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pubmed:owner |
NLM
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pubmed:authorsComplete |
N
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pubmed:pagination |
892-8
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pubmed:dateRevised |
2010-9-7
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pubmed:meshHeading |
|
